Evidence map›Paper›PMID 33207200›Full record

ArticleCell reports2020

RACK1 Mediates NLRP3 Inflammasome Activation by Promoting NLRP3 Active Conformation and Inflammasome Assembly.

Yanhui Duan, Lingzhi Zhang, Diego Angosto-Bazarra, Pablo Pelegrín, Gabriel Núñez, Yuan He

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
3.5field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

51 citing papers in PubMed, 69 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

Yanhui DuanDepartment of Biochemistry, Microbiology and Immunology, Wayne State University School of Medicine, Detroit, MI 48201, USA.
Lingzhi ZhangDepartment of Pathology and Rogel Cancer Center, University of Michigan Medical School, Ann Arbor, MI 48109, USA.
Diego Angosto-BazarraInstituto Murciano de Investigación Biosanitaria IMIB-Arrixaca, Hospital Clínico Universitario Virgen de la Arrixaca, Murcia, Spain.
Pablo PelegrínInstituto Murciano de Investigación Biosanitaria IMIB-Arrixaca, Hospital Clínico Universitario Virgen de la Arrixaca, Murcia, Spain.
Gabriel NúñezDepartment of Pathology and Rogel Cancer Center, University of Michigan Medical School, Ann Arbor, MI 48109, USA. Electronic address: gabriel.nunez@umich.edu.
Yuan HeDepartment of Biochemistry, Microbiology and Immunology, Wayne State University School of Medicine, Detroit, MI 48201, USA. Electronic address: yhe@med.wayne.edu.
Instituto Murciano de Investigación Biosanitaria · ESUniversity of Michigan–Ann Arbor · USWayne State University · US

Funding

Cryopyrin/NLRP3 Signaling in Inflammation and Innate ImmunityR37AI063331 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NUNEZ, GABRIEL · 2016 to 2025
$3.9M
Molecular mechanism of NLRP3 inflammasome activationR01AI148544 · NIAID · WAYNE STATE UNIVERSITY · PI HE, YUAN · 2020 to 2025
$1.9M
Cryopyrin/NLRP3 Signaling in Inflammation and Innate ImmunityR56AI063331 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI NUNEZ, GABRIEL · 2010 to 2010
$386k
NIAID NIH HHS R01 AI148544NIAID NIH HHS R37 AI063331NIAID NIH HHS R56 AI063331
6 · The paper itself

Abstract

The NLRP3 inflammasome, a critical component of the innate immune system, induces caspase-1 activation and interleukin (IL)-1β maturation in response to microbial infection and cellular damage. However, aberrant activation of the NLRP3 inflammasome contributes to the pathogenesis of several inflammatory disorders, including cryopyrin-associated periodic syndromes, Alzheimer's disease, type 2 diabetes, and atherosclerosis. Here, we identify the receptor for activated protein C kinase 1 (RACK1) as a component of the NLRP3 complexes in macrophages. RACK1 interacts with NLRP3 and NEK7 but not ASC. Suppression of RACK1 expression abrogates caspase-1 activation and IL-1β release in response to NLRP3- but not NLRC4- or AIM2-activating stimuli. This RACK1 function is independent of its ribosomal binding activity. Mechanistically, RACK1 promotes the active conformation of NLRP3 induced by activating stimuli and subsequent inflammasome assembly. These results demonstrate that RACK1 is a critical mediator for NLRP3 inflammasome activation.

Indexed as

AnimalsCARD Signaling Adaptor ProteinsCaspase 1FemaleHEK293 CellsHumansInflammasomesInterleukin-1betaMacrophagesMaleMiceMice, Inbred C57BLNIMA-Related KinasesNLR Family, Pyrin Domain-Containing 3 ProteinReceptors for Activated C KinaseCARD Signaling Adaptor ProteinsCaspase 1InflammasomesInterleukin-1betaNIMA-Related KinasesNLR Family, Pyrin Domain-Containing 3 ProteinReceptors for Activated C KinaseCaspase-1IL-1βNEK7NLRP3 inflammasomeRACK1

Identifiers

PMID33207200
PMCPMC7709964
OpenAlexW3101510090

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.